Human anamorsin was implicated in cytosolic iron-sulfur (Fe/S) protein biogenesis. Here, the structural and metal-binding properties of anamorsin and its interaction with Mia40, a well-known oxidoreductase involved in protein trapping in the mitochondrial intermembrane space (IMS), were characterized. We show that (1), anamorsin contains two structurally independent domains connected by an unfolded linker; (2), the C-terminal domain binds a [2Fe-2S] cluster through a previously unknown cysteine binding motif in Fe/S proteins; (3), Mia40 specifically introduces two disulfide bonds in a twin CX(2)C motif of the C-terminal domain; (4), anamorsin and Mia40 interact through an intermolecular disulfide-bonded intermediate; and (5), anamorsin is imported into mitochondria. Hence, anamorsin is the first identified Fe/S protein imported into the IMS, raising the possibility that it plays a role in cytosolic Fe/S cluster biogenesis also once trapped in the IMS.

Anamorsin Is a [2Fe-2S] Cluster-Containing Substrate of the Mia40-Dependent Mitochondrial Protein Trapping Machinery / L.Banci; I.Bertini; S.Ciofi-Baffoni; F.Boscaro; A.Chatzi; M.Mikolajczyk; K.Tokatlidis; J.Winkelmann. - In: CHEMISTRY & BIOLOGY. - ISSN 1074-5521. - STAMPA. - 18(6):(2011), pp. 794-804. [10.1016/j.chembiol.2011.03.015]

Anamorsin Is a [2Fe-2S] Cluster-Containing Substrate of the Mia40-Dependent Mitochondrial Protein Trapping Machinery

BANCI, LUCIA;BERTINI, IVANO;CIOFI BAFFONI, SIMONE;BOSCARO, FRANCESCA;MIKOLAJCZYK, MACIEJ;WINKELMANN, JULIA
2011

Abstract

Human anamorsin was implicated in cytosolic iron-sulfur (Fe/S) protein biogenesis. Here, the structural and metal-binding properties of anamorsin and its interaction with Mia40, a well-known oxidoreductase involved in protein trapping in the mitochondrial intermembrane space (IMS), were characterized. We show that (1), anamorsin contains two structurally independent domains connected by an unfolded linker; (2), the C-terminal domain binds a [2Fe-2S] cluster through a previously unknown cysteine binding motif in Fe/S proteins; (3), Mia40 specifically introduces two disulfide bonds in a twin CX(2)C motif of the C-terminal domain; (4), anamorsin and Mia40 interact through an intermolecular disulfide-bonded intermediate; and (5), anamorsin is imported into mitochondria. Hence, anamorsin is the first identified Fe/S protein imported into the IMS, raising the possibility that it plays a role in cytosolic Fe/S cluster biogenesis also once trapped in the IMS.
2011
18(6)
794
804
L.Banci; I.Bertini; S.Ciofi-Baffoni; F.Boscaro; A.Chatzi; M.Mikolajczyk; K.Tokatlidis; J.Winkelmann
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/454258
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